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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Journal of the Ameri...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Journal of the American Oil Chemists Society
Article . 1973 . Peer-reviewed
License: Wiley Online Library User Agreement
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Reaction of autoxidizing linoleate with coho salmon myosin

Authors: R J, Braddock; L R, Dugan;

Reaction of autoxidizing linoleate with coho salmon myosin

Abstract

AbstractReactions that contribute to denaturation, destruction and quality changes of fish muscle lipids and protein were studied. Compounds with characteristic fluorescence spectra were isolated by extraction and thin layer chromatography from an autoxidizing system consisting of sodium linoleate, Coho salmon myosin and buffer. Similar compounds were also present in extracts from freeze‐dried salmon steaks and salmon kept frozen at −20 C for 1 year. TBA values and oxygen uptake of the autoxidizing system showed initial rapid increases with time followed by a significant decrease in TBA values and gradual leveling off of oxygen uptake upon prolonged oxidation. IR spectra before and after borohydride reduction and UV, visible and fluorescence spectra indicated the presence of C=N functional groups in extracts from the various samples. These compounds were not extractable from the control myosin solutions allowed to oxidize without addition of linoleate. Amino acid analyses of the myosin from the autoxidizing system, when compared with nonoxidized myosin‐linoleate systems, indicated significant decreases in the amounts of histidine, lysine and methionine following oxidation. These reactions apparently contribute to the denaturation and destruction of the lipids and protein in the model system, as well as in a frozen or freeze‐dried product.

Related Organizations
Keywords

Protein Denaturation, Chemical Phenomena, Spectrophotometry, Infrared, Muscle Proteins, Myosins, Lipids, Chemistry, Oxygen Consumption, Spectrometry, Fluorescence, Linoleic Acids, Salmon, Fish Products, Animals, Chromatography, Thin Layer, Amino Acids, Oxidation-Reduction

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    influence
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Powered by OpenAIRE graph
Found an issue? Give us feedback
selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
53
Average
Top 10%
Top 10%
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